GUN2_BACSU
ID GUN2_BACSU Reviewed; 499 AA.
AC P10475;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Endoglucanase;
DE EC=3.2.1.4;
DE AltName: Full=Carboxymethyl-cellulase;
DE Short=CMCase;
DE Short=Cellulase;
DE AltName: Full=Endo-1,4-beta-glucanase;
DE Flags: Precursor;
GN Name=eglS; Synonyms=bglC, gld; OrderedLocusNames=BSU18130;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAP115;
RX PubMed=3024130; DOI=10.1093/nar/14.22.9159;
RA Mackay R.M., Lo A., Willick G., Zuker M., Baird S., Dove M., Moranelli F.,
RA Seligy V.;
RT "Structure of a Bacillus subtilis endo-beta-1,4-glucanase gene.";
RL Nucleic Acids Res. 14:9159-9170(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CK-2;
RX PubMed=7710280; DOI=10.1007/bf00882768;
RA Lindahl V., Aa K., Tronsmo A.;
RT "Nucleotide sequence of an endo-beta-1,4-glucanase gene from Bacillus
RT subtilis CK-2.";
RL Antonie Van Leeuwenhoek 66:327-332(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969507; DOI=10.1099/13500872-142-11-3097;
RA Rose M., Entian K.-D.;
RT "New genes in the 170 degrees region of the Bacillus subtilis genome encode
RT DNA gyrase subunits, a thioredoxin, a xylanase and an amino acid
RT transporter.";
RL Microbiology 142:3097-3101(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [5]
RP PROTEIN SEQUENCE OF 30-45.
RC STRAIN=CK-2;
RX PubMed=7710279; DOI=10.1007/bf00882767;
RA Aa K., Flengsrud R., Lindahl V., Tronsmo A.;
RT "Characterization of production and enzyme properties of an endo-beta-1,4-
RT glucanase from Bacillus subtilis CK-2 isolated from compost soil.";
RL Antonie Van Leeuwenhoek 66:319-326(1994).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA97610.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z29076; CAA82317.1; -; Genomic_DNA.
DR EMBL; X04689; CAA28392.1; -; Genomic_DNA.
DR EMBL; X67044; CAA47429.1; -; Genomic_DNA.
DR EMBL; Z73234; CAA97610.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB13696.2; -; Genomic_DNA.
DR PIR; G69593; G69593.
DR RefSeq; NP_389695.2; NC_000964.3.
DR RefSeq; WP_003231540.1; NZ_JNCM01000035.1.
DR PDB; 2L8A; NMR; -; A=354-499.
DR PDB; 3PZT; X-ray; 1.97 A; A/B=27-332.
DR PDB; 3PZU; X-ray; 2.10 A; A/B=27-332.
DR PDB; 3PZV; X-ray; 2.87 A; A/B/C/D=27-332.
DR PDB; 6UFV; X-ray; 1.06 A; A=354-499.
DR PDB; 6UFW; X-ray; 1.28 A; A=354-499.
DR PDBsum; 2L8A; -.
DR PDBsum; 3PZT; -.
DR PDBsum; 3PZU; -.
DR PDBsum; 3PZV; -.
DR PDBsum; 6UFV; -.
DR PDBsum; 6UFW; -.
DR AlphaFoldDB; P10475; -.
DR BMRB; P10475; -.
DR SMR; P10475; -.
DR STRING; 224308.BSU18130; -.
DR CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR PaxDb; P10475; -.
DR PRIDE; P10475; -.
DR EnsemblBacteria; CAB13696; CAB13696; BSU_18130.
DR GeneID; 938607; -.
DR KEGG; bsu:BSU18130; -.
DR PATRIC; fig|224308.179.peg.1977; -.
DR eggNOG; COG2730; Bacteria.
DR InParanoid; P10475; -.
DR OMA; NVMYALH; -.
DR BioCyc; BSUB:BSU18130-MON; -.
DR BRENDA; 3.2.1.4; 658.
DR EvolutionaryTrace; P10475; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.710; -; 1.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00942; CBM_3; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM01067; CBM_3; 1.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51172; CBM3; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Direct protein sequencing; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:7710279"
FT CHAIN 30..499
FT /note="Endoglucanase"
FT /id="PRO_0000007840"
FT DOMAIN 350..499
FT /note="CBM3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT ACT_SITE 169
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT ACT_SITE 257
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 69..70
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 263..264
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 296..298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT CONFLICT 283
FT /note="S -> N (in Ref. 2; CAA47429)"
FT /evidence="ECO:0000305"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:3PZU"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:3PZT"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:3PZT"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:3PZT"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:3PZT"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3PZT"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:3PZT"
FT STRAND 89..98
FT /evidence="ECO:0007829|PDB:3PZT"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:3PZT"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:3PZT"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:3PZT"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:3PZT"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:3PZT"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:3PZT"
FT HELIX 142..156
FT /evidence="ECO:0007829|PDB:3PZT"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:3PZT"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:3PZT"
FT HELIX 180..194
FT /evidence="ECO:0007829|PDB:3PZT"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:3PZT"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:3PZT"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:3PZT"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:3PZT"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:3PZT"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:3PZT"
FT HELIX 237..248
FT /evidence="ECO:0007829|PDB:3PZT"
FT STRAND 253..261
FT /evidence="ECO:0007829|PDB:3PZT"
FT HELIX 271..283
FT /evidence="ECO:0007829|PDB:3PZT"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:3PZT"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:3PZT"
FT HELIX 320..330
FT /evidence="ECO:0007829|PDB:3PZT"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:6UFV"
FT STRAND 372..378
FT /evidence="ECO:0007829|PDB:6UFV"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:6UFV"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:6UFV"
FT STRAND 389..395
FT /evidence="ECO:0007829|PDB:6UFV"
FT STRAND 402..409
FT /evidence="ECO:0007829|PDB:6UFV"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:6UFV"
FT STRAND 416..427
FT /evidence="ECO:0007829|PDB:6UFV"
FT STRAND 430..440
FT /evidence="ECO:0007829|PDB:6UFV"
FT STRAND 447..450
FT /evidence="ECO:0007829|PDB:2L8A"
FT STRAND 452..458
FT /evidence="ECO:0007829|PDB:6UFV"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:6UFV"
FT STRAND 482..488
FT /evidence="ECO:0007829|PDB:6UFV"
FT STRAND 491..495
FT /evidence="ECO:0007829|PDB:6UFV"
SQ SEQUENCE 499 AA; 55287 MW; 8F735FF711B3EAE2 CRC64;
MKRSISIFIT CLLITLLTMG GMIASPASAA GTKTPVAKNG QLSIKGTQLV NRDGKAVQLK
GISSHGLQWY GEYVNKDSLK WLRDDWGITV FRAAMYTADG GYIDNPSVKN KVKEAVEAAK
ELGIYVIIDW HILNDGNPNQ NKEKAKEFFK EMSSLYGNTP NVIYEIANEP NGDVNWKRDI
KPYAEEVISV IRKNDPDNII IVGTGTWSQD VNDAADDQLK DANVMYALHF YAGTHGQFLR
DKANYALSKG APIFVTEWGT SDASGNGGVF LDQSREWLKY LDSKTISWVN WNLSDKQESS
SALKPGASKT GGWRLSDLSA SGTFVRENIL GTKDSTKDIP ETPSKDKPTQ ENGISVQYRA
GDGSMNSNQI RPQLQIKNNG NTTVDLKDVT ARYWYKAKNK GQNFDCDYAQ IGCGNVTHKF
VTLHKPKQGA DTYLELGFKN GTLAPGASTG NIQLRLHNDD WSNYAQSGDY SFFKSNTFKT
TKKITLYDQG KLIWGTEPN